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| | ==Monoclinic Crystal Structure of EutL from Clostridium Perfringens== | | ==Monoclinic Crystal Structure of EutL from Clostridium Perfringens== |
| - | <StructureSection load='4tlh' size='340' side='right' caption='[[4tlh]], [[Resolution|resolution]] 1.70Å' scene=''> | + | <StructureSection load='4tlh' size='340' side='right'caption='[[4tlh]], [[Resolution|resolution]] 1.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4tlh]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Clostridium_perfringens_e_str._jgs1987 Clostridium perfringens e str. jgs1987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TLH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4TLH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4tlh]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens_E_str._JGS1987 Clostridium perfringens E str. JGS1987]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4TLH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4TLH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">eutL, AC3_1081 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=451755 Clostridium perfringens E str. JGS1987])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4tlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tlh OCA], [http://pdbe.org/4tlh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4tlh RCSB], [http://www.ebi.ac.uk/pdbsum/4tlh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4tlh ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4tlh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4tlh OCA], [https://pdbe.org/4tlh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4tlh RCSB], [https://www.ebi.ac.uk/pdbsum/4tlh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4tlh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/EUTL_CLOPE EUTL_CLOPE] A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. May be involved in cofactor diffusion across the BMC (Probable). Cobalamin is covalently bound to 1 subunit of the trimer on the concave (lumenal) face in a closed pore conformation; whether this is physiologically relevant is unclear (PubMed:25484204). The closed form has 3 very narrow channels (1.3 Angstrom at their narrowest) per trimer lined by acidic and aromatic residues; 2 ethanolamine molecules can bind in each channel, on either side of the constriction. Does not bind acetate, ethanol or acetyl phosphate, all of which are small molecules involved in ethanolamine metabolism (PubMed:25752492). Ethanolamine-binding has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (Probable).<ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:25484204</ref> <ref>PMID:25752492</ref> <ref>PMID:29717712</ref> |
| | + | == References == |
| | + | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Clostridium perfringens e str. jgs1987]] | + | [[Category: Clostridium perfringens E str. JGS1987]] |
| - | [[Category: Thompson, M C]] | + | [[Category: Large Structures]] |
| - | [[Category: Yeates, T O]] | + | [[Category: Thompson MC]] |
| - | [[Category: Bacterial microcompartment]] | + | [[Category: Yeates TO]] |
| - | [[Category: Bmc shell protein]]
| + | |
| - | [[Category: Ethanolamine]]
| + | |
| - | [[Category: Eut]]
| + | |
| - | [[Category: Microcrystallography]]
| + | |
| - | [[Category: Structural polymorphism]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
EUTL_CLOPE A component of the bacterial microcompartment (BMC) shell dedicated to ethanolamine degradation. May be involved in cofactor diffusion across the BMC (Probable). Cobalamin is covalently bound to 1 subunit of the trimer on the concave (lumenal) face in a closed pore conformation; whether this is physiologically relevant is unclear (PubMed:25484204). The closed form has 3 very narrow channels (1.3 Angstrom at their narrowest) per trimer lined by acidic and aromatic residues; 2 ethanolamine molecules can bind in each channel, on either side of the constriction. Does not bind acetate, ethanol or acetyl phosphate, all of which are small molecules involved in ethanolamine metabolism (PubMed:25752492). Ethanolamine-binding has been hypothesized to stabilize the EutL central pore in a closed (non-transporting) state. An open pore is thought to be large enough to transport ATP and/or cobalamin (Probable).[1] [2] [3] [4] [5]
References
- ↑ Thompson MC, Crowley CS, Kopstein J, Bobik TA, Yeates TO. Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor. Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1584-90. doi:, 10.1107/S2053230X1402158X. Epub 2014 Nov 14. PMID:25484204 doi:http://dx.doi.org/10.1107/S2053230X1402158X
- ↑ Thompson MC, Cascio D, Leibly DJ, Yeates TO. An allosteric model for control of pore opening by substrate binding in the eutl microcompartment shell protein. Protein Sci. 2015 Mar 9. doi: 10.1002/pro.2672. PMID:25752492 doi:http://dx.doi.org/10.1002/pro.2672
- ↑ Thompson MC, Crowley CS, Kopstein J, Bobik TA, Yeates TO. Structure of a bacterial microcompartment shell protein bound to a cobalamin cofactor. Acta Crystallogr F Struct Biol Commun. 2014 Dec 1;70(Pt 12):1584-90. doi:, 10.1107/S2053230X1402158X. Epub 2014 Nov 14. PMID:25484204 doi:http://dx.doi.org/10.1107/S2053230X1402158X
- ↑ Thompson MC, Cascio D, Leibly DJ, Yeates TO. An allosteric model for control of pore opening by substrate binding in the eutl microcompartment shell protein. Protein Sci. 2015 Mar 9. doi: 10.1002/pro.2672. PMID:25752492 doi:http://dx.doi.org/10.1002/pro.2672
- ↑ Thompson MC, Cascio D, Yeates TO. Microfocus diffraction from different regions of a protein crystal: structural variations and unit-cell polymorphism. Acta Crystallogr D Struct Biol. 2018 May 1;74(Pt 5):411-421. doi:, 10.1107/S2059798318003479. Epub 2018 Apr 24. PMID:29717712 doi:http://dx.doi.org/10.1107/S2059798318003479
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